ID   UGT13_HORVV             Reviewed;         475 AA.
AC   M0Y4P1; D3WYW2;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=UDP-glucosyltransferase UGT13248 {ECO:0000305};
DE            Short=HvUGT13248 {ECO:0000303|PubMed:20521959};
DE            EC=2.4.1.- {ECO:0000269|PubMed:20521959};
DE   AltName: Full=Deoxynivalenol-UDP-glucosyltransferase {ECO:0000303|PubMed:20521959};
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Spike;
RX   PubMed=20521959; DOI=10.1094/mpmi-23-7-0977;
RA   Schweiger W., Boddu J., Shin S., Poppenberger B., Berthiller F.,
RA   Lemmens M., Muehlbauer G.J., Adam G.;
RT   "Validation of a candidate deoxynivalenol-inactivating UDP-
RT   glucosyltransferase from barley by heterologous expression in yeast.";
RL   Mol. Plant Microbe Interact. 23:977-986(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23075845; DOI=10.1038/nature11543;
RG   International Barley Genome Sequencing Consortium;
RA   Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA   Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT   "A physical, genetic and functional sequence assembly of the barley
RT   genome.";
RL   Nature 491:711-716(2012).
CC   -!- FUNCTION: Involved in the detoxification of the Fusarium mycotoxin
CC       deoxynivalenol by the transfer of glucose from UDP-D-glucose to the
CC       hydroxyl group at C-3, forming deoxynivalenol-3-O-beta-D-glucoside.
CC       {ECO:0000269|PubMed:20521959}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; GU170355; ADC92550.1; -; mRNA.
DR   AlphaFoldDB; M0Y4P1; -.
DR   SMR; M0Y4P1; -.
DR   STRING; 4513.MLOC_65675.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; M0Y4P1; -.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0384710.1; HORVU.MOREX.r2.5HG0384710.1; HORVU.MOREX.r2.5HG0384710.
DR   EnsemblPlants; HORVU.MOREX.r3.5HG0464880.1; HORVU.MOREX.r3.5HG0464880.1; HORVU.MOREX.r3.5HG0464880.
DR   Gramene; HORVU.MOREX.r2.5HG0384710.1; HORVU.MOREX.r2.5HG0384710.1; HORVU.MOREX.r2.5HG0384710.
DR   Gramene; HORVU.MOREX.r3.5HG0464880.1; HORVU.MOREX.r3.5HG0464880.1; HORVU.MOREX.r3.5HG0464880.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; M0Y4P1; -.
DR   OMA; RNATRLM; -.
DR   Proteomes; UP000011116; Unassembled WGS sequence.
DR   ExpressionAtlas; M0Y4P1; baseline and differential.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0098754; P:detoxification; IDA:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Detoxification; Glycosyltransferase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..475
FT                   /note="UDP-glucosyltransferase UGT13248"
FT                   /id="PRO_0000441956"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         152
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         299
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         352
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         369..377
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   BINDING         393..394
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XT97"
FT   CONFLICT        271
FT                   /note="F -> L (in Ref. 1; ADC92550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="D -> E (in Ref. 1; ADC92550)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   475 AA;  51636 MW;  1D66662961998348 CRC64;
     METTVTAVSG TTSSSVGHGA GGGAARVLLL PSPGAQGHTN PMLQLGRRLA YHGLRPTLVA
     TRYVLSTTPA PGAPFDVAAI SDGFDAGGMA LCPDPAEYFS RLEAVGSETL RELLLSEARA
     GRPVRVLVYD AHLAWARRVA QASGVAAAAF FSQPCSVDVV YGELWAGRLA LPATDGRALL
     ARGVLGVELG LEDMPPFAAV PESQPAFLQV SVGQFEGLDY ADDVLVNSFR DIEPKEVEYM
     ELTWRAKMVG PTLPSYYLGD GRLPSNKSYG FDLFNSDVEC MDWLEKQMNS SVVLVSYGTV
     SNYDATQLEE LGNGLCNSSK PFLWVVRSNE EHKLSEELKE KCGKIGLIVS WCPQLEVLAH
     RAIGCFVTHC GWNSTLEALV NGVPFVGIPH WADQPTIAKY VESAWGMGVR ARKNKNGCLK
     KEEVERCIRE VMDGERKDEY KKNAMNWMQK AKEAMQEGGS SDKHVAEFAT KYSSI